ID A0A162UV58_PHYB8 Unreviewed; 1619 AA.
AC A0A162UV58;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE RecName: Full=1,3-beta-glucan synthase {ECO:0000256|ARBA:ARBA00012589};
DE EC=2.4.1.34 {ECO:0000256|ARBA:ARBA00012589};
GN ORFNames=PHYBLDRAFT_57959 {ECO:0000313|EMBL:OAD78252.1};
OS Phycomyces blakesleeanus (strain ATCC 8743b / DSM 1359 / FGSC 10004 / NBRC
OS 33097 / NRRL 1555).
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC Mucoromycetes; Mucorales; Phycomycetaceae; Phycomyces.
OX NCBI_TaxID=763407 {ECO:0000313|EMBL:OAD78252.1, ECO:0000313|Proteomes:UP000077315};
RN [1] {ECO:0000313|Proteomes:UP000077315}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL 1555(-) {ECO:0000313|Proteomes:UP000077315};
RG DOE Joint Genome Institute;
RA Corrochano L.M., Kuo A., Marcet-Houben M., Polaino S., Salamov A.,
RA Villalobos J.M., Alvarez M.I., Avalos J., Benito E.P., Benoit I.,
RA Burger G., Camino L.P., Canovas D., Cerda-Olmedo E., Cheng J.-F.,
RA Dominguez A., Elias M., Eslava A.P., Glaser F., Grimwood J., Gutierrez G.,
RA Heitman J., Henrissat B., Iturriaga E.A., Lang B.F., Lavin J.L., Lee S.,
RA Li W., Lindquist E., Lopez-Garcia S., Luque E.M., Marcos A.T., Martin J.,
RA McCluskey K., Medina H.R., Miralles-Duran A., Miyazaki A., Munoz-Torres E.,
RA Oguiza J.A., Ohm R., Olmedo M., Orejas M., Ortiz-Castellanos L.,
RA Pisabarro A.G., Rodriguez-Romero J., Ruiz-Herrera J., Ruiz-Vazquez R.,
RA Sanz C., Schackwitz W., Schmutz J., Shahriari M., Shelest E.,
RA Silva-Franco F., Soanes D., Syed K., Tagua V.G., Talbot N.J., Thon M.,
RA De vries R.P., Wiebenga A., Yadav J.S., Braun E.L., Baker S., Garre V.,
RA Horwitz B., Torres-Martinez S., Idnurm A., Herrera-Estrella A.,
RA Gabaldon T., Grigoriev I.V.;
RT "Expansion of signal transduction pathways in fungi by whole-genome
RT duplication.";
RL Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[(1->3)-beta-D-glucosyl](n) + UDP-alpha-D-glucose = [(1->3)-
CC beta-D-glucosyl](n+1) + H(+) + UDP; Xref=Rhea:RHEA:21476, Rhea:RHEA-
CC COMP:11146, Rhea:RHEA-COMP:14303, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:37671, ChEBI:CHEBI:58223, ChEBI:CHEBI:58885; EC=2.4.1.34;
CC Evidence={ECO:0000256|ARBA:ARBA00000192};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 48 family.
CC {ECO:0000256|ARBA:ARBA00009040}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KV440973; OAD78252.1; -; Genomic_DNA.
DR RefSeq; XP_018296292.1; XM_018440265.1.
DR STRING; 763407.A0A162UV58; -.
DR GeneID; 29001171; -.
DR VEuPathDB; FungiDB:PHYBL_57959; -.
DR InParanoid; A0A162UV58; -.
DR OrthoDB; 354539at2759; -.
DR Proteomes; UP000077315; Unassembled WGS sequence.
DR GO; GO:0000148; C:1,3-beta-D-glucan synthase complex; IEA:InterPro.
DR GO; GO:0003843; F:1,3-beta-D-glucan synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0006075; P:(1->3)-beta-D-glucan biosynthetic process; IEA:InterPro.
DR InterPro; IPR026899; FKS1-like_dom1.
DR InterPro; IPR003440; Glyco_trans_48.
DR PANTHER; PTHR12741:SF29; 1,3-BETA-GLUCAN SYNTHASE COMPONENT FKS1-RELATED; 1.
DR PANTHER; PTHR12741; LYST-INTERACTING PROTEIN LIP5 DOPAMINE RESPONSIVE PROTEIN DRG-1; 1.
DR Pfam; PF14288; FKS1_dom1; 1.
DR Pfam; PF02364; Glucan_synthase; 1.
DR SMART; SM01205; FKS1_dom1; 1.
PE 3: Inferred from homology;
KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000077315};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 238..260
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 281..303
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 323..342
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 349..370
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 406..429
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 450..477
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 483..506
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1084..1109
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1140..1157
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1231..1249
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1255..1271
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1340..1364
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1384..1416
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1428..1450
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1530..1549
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1583..1607
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 95..204
FT /note="1,3-beta-glucan synthase component FKS1-like"
FT /evidence="ECO:0000259|SMART:SM01205"
FT REGION 845..864
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1619 AA; 186239 MW; EEA848F9AFE75EF4 CRC64;
MYDHLMTMLD SRASRMSPKL ALLTIHAEYI GGPDANYRKW YFAAQLDLND VTDEKNVATD
TVETSKDSKS NISQAHRLKE TKEAWRIKME RMKDEERIQQ LALWLLLWAE ASVIRFCPEV
LCFIFKLAED HWENRTDKGV PAGTYLDTVI TPLYNFIRDQ SYRPMEDGRY TERERDHACV
IGYDDVNQQF WYPEKIALLR LNDKRKLVDL HPSERYQALG DMDWNHSFQK TFKEKRSWMH
MAVNFTRIWI IHIVTFWYYI SANAGDLYLS TDKDEAKTET PVKLSVVALG GAIATLLVML
GSLVEYMYVP MSWYGARILS RRFAMLFGIL VLNTGPSFYC VFFDRTSRIS LAVSAAQLFI
SVITSLYFSI MPQSQLFVRH KKDSRRMLAS QTFTANFPPL KRMDRLISVG LWSCVFICKL
LESYFFLALS FKDPLRIMSS MQIQDCRDPI IGTELCVLMP SFTLGLMLLM ALVLFFLDTY
LWYVVWNTVF SVARSFYLGI SIWTPWRNIF SRLPKRIYAK ILAGSEIGAH YKPKFLYSQV
WNAFVISMYR EHLLSPDHIT KLLYQRVPNA ENGKFTLKSP TFFETQEDIA FKTEYYPQES
EAERRMQFFA QSMTTPMPDP LPVQKMPTFT VMTPHYGEKI IFSLREIIRE EDKNTRITLL
EYLKKLHPFE WDNFVKDTKV LVDETSLSNS GGEEDTAMAE DISIDDLPFY CVGFKSSAPE
YTLRTRIWAS LRSQTLYRTI TGFMNYQSAL KLLYRVENPE LVTDSINFEK LESDLEQMAN
RKFRFLIAMQ RYASFDKEEL ENVDYVLKAY PNLQIAYLEE EKSQDEDGKK KNTFYSVLID
GHSTVGSDGK RTPKYRVRLP GNPILGDGKS DNQNTALIYY RGEYLQLVDA NQDNYLEECL
KIRNVLSEFE NLSVSNESPY ADVGFSTGPV AIVGAREYIF SENIGVLGDV AAGKEQTFGT
LTQRIMATIG GKLHYGHPDF LNAIFMTTRG GVSKAQKGLH LNEDIYAGMN AFERGGRIKH
IEYYQCGKGR DLGFGSILNF VTKIGTGMGE QMLSREYYYI GTQLPLDRFL TFYYAHPGFH
INNIFIMLSV HMFMIVLLFL ASMSVPLLVC EFDKDAPPEA PRTPDGCYDL VPIYNWLKRV
VISIFAVFFI SFLPLFLQEL TERGFMRATS RLCKHIISLS PFFEIFVTQT YASAILNNLT
FGGARYIGTG RGFATTRLPF SLLYSRFADS SIYVGARSTL ILLFGSLIIW APHYIYFWIT
VIALMMSPFL FNPHQFSMGD FIIDYRELLR WLSRGNGKTH ASSWIGYCRF SRMRTTGVKI
RQLGDAPKAW NKQHQSRARF GVIFFSEIAV PFFLAVGCVV AYLFTRSFDM SEGHNAGQEA
PSGLIRIAAI AVLPLILNAG VLVALFCVSL LGGILASLCC SVKFGATVAG AAHAWAVINF
IGFFELFYFL EKWNLSRTIL GMIAVSSVQR FIFKLITVCL LTREFQQDGS NQGWWTGRWY
GRGLGWYVIT QPLREFVCKV VEMSLFAADF VLTHFIMIFL FLICFVPGIN KWHSLMLFWL
KPSMQIREPI YSTAQRQKRR RICILYGFLL TCFALLFFGL LIAPSIIGSR LEFKLDLPI
//
